Linked Life Data

6295491

Source:http://linkedlifedata.com/resource/pubmed/id/6295491

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-3-24
pubmed:abstractText
Peroxidation of SCN- to OSCN-, catalysed by myeloperoxidase and lactoperoxidase, was studied. The rate of this reaction showed sharp optima between pH 5 and 7.5, the position of which is determined by the concentrations of both SCN- and H2O2. At low pH values, both SCN- and H+ inhibited myeloperoxidase and lactoperoxidase competitively with respect to H2O2. The inhibition constants of SCN- for myeloperoxidase and lactoperoxidase (2 and 6 mM, respectively) are independent of pH. For these enzymes a Ki for H+ of 1 microM was found that corresponded to an ionisable group on the enzymes (pKa = 6) which controls the enzymic activity. A kinetic expression is proposed that explains most of the data. The physiological consequences of the corresponding mechanism are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
709
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
212-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't